ISPE_CHLL2
ID ISPE_CHLL2 Reviewed; 288 AA.
AC B3EE40;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; OrderedLocusNames=Clim_1700;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-
CC Rule:MF_00061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00061};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6. {ECO:0000255|HAMAP-Rule:MF_00061}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00061}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001097; ACD90742.1; -; Genomic_DNA.
DR RefSeq; WP_012466615.1; NC_010803.1.
DR AlphaFoldDB; B3EE40; -.
DR SMR; B3EE40; -.
DR STRING; 290315.Clim_1700; -.
DR EnsemblBacteria; ACD90742; ACD90742; Clim_1700.
DR KEGG; cli:Clim_1700; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_3_0_10; -.
DR OMA; RWPSPAK; -.
DR OrthoDB; 1938933at2; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000008841; Chromosome.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00061; IspE; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF010376; IspE; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_1000092070"
FT ACT_SITE 11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 93..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ SEQUENCE 288 AA; 31582 MW; B6C39F72B9529274 CRC64;
MLPVSVKSFA KINLGLLITS KRSDGYHTLE TVFAPIDWYD TLEFSPSDTL SMCCTDSALP
VDENNLCMRA AKALQESAGC STGVSITLDK RIPFGAGLGG GSSDAATVLG MLNEFWNVRA
SLADLHILAV RLGADVPYFL EMKGLAFAKG IGDELEDLSL RLPFHIVTVF PEVHISTVWA
YKHFYPRFER TSPDLRPLVT ALCLEGERSC LGAFENDFEP AVFDHYPGVK KVKQDLLDSG
SFFASLSGSG SAVFGFFDKR EDADDALMMM REQGFRTSIT APDFSMVR